Name
MBL-C, Mouse, mAb 14D12
Catalog nr
HM1038
(lot number and expiry date are indicated on the label)
Short description
Mannose binding lectin (MBL), also called mannose- or mannan-binding protein (MBP), is a member of the group of collectins. MBL is an important pattern-recognition receptor in the innate immune system. The protein mediates innate immune responses, such as activation of the complement lectin pathway and phagocytosis, to help fight infections. MBL is an oligomeric ...
Size
100 µg
Application
F
,
IA
,
IF
,
W
Technical datasheet
Description
Mannose binding lectin (MBL), also called mannose- or mannan-binding protein (MBP), is a member of the group of collectins. MBL is an important pattern-recognition receptor in the innate immune system. The protein mediates innate immune responses, such as activation of the complement lectin pathway and phagocytosis, to help fight infections. MBL is an oligomeric lectin that recognizes carbohydrates as mannose and N-acetylglucosamine on pathogens. MBL contains a cysteine rich, a collagen like and a carbohydrate recognition domain. Binding of MBL leads to the activation of MBL-associated serine proteases (MASP's). Activated MASP-2 cleaves C4 and C2 in a similar way as C1s do for the classical pathway (CP) leading to the formation of C4b2a, cleavage of the classical pathway convertase C3, and eventually complement activation up to the formation of the membrane attack complex. MBL is able to activate the complement pathway independent of the classical and alternative complement activation pathways.
MBL is predominantly synthesized by hepatocytes and has been isolated from the liver or serum of several vertebrate species. Only one form of human MBL has been characterized, while two forms are found in rhesus monkeys, rabbits, rats and mice. The mouse forms are known as MBL-A and MBL-C.
The MBL-C concentrations in serum are about 6-fold compared to that of MBL-A. MBL-A, but not MBL-C, was found to be an acute phase protein in casein and LPS-injection models. MBL-C exists in higher oligomeric forms than MBL-A. The monoclonal antibody 14D12 is a calcium-dependent antibody.
.
MBL is predominantly synthesized by hepatocytes and has been isolated from the liver or serum of several vertebrate species. Only one form of human MBL has been characterized, while two forms are found in rhesus monkeys, rabbits, rats and mice. The mouse forms are known as MBL-A and MBL-C.
The MBL-C concentrations in serum are about 6-fold compared to that of MBL-A. MBL-A, but not MBL-C, was found to be an acute phase protein in casein and LPS-injection models. MBL-C exists in higher oligomeric forms than MBL-A. The monoclonal antibody 14D12 is a calcium-dependent antibody.
.
Immunogen
Purified MBL-C
Formulation
1 ml (100 µg/ml) 0.2 µm filtered antibody solution in PBS, containing 0.02% sodium azide and 0.1% bovine serum albumin.
Species
Rat IgG2a
Application
|
|
F4 |
FC |
FS |
IA1 |
IF3,5 |
IP |
P |
W1,2 |
|
Yes |
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● |
● |
|
|
● |
|
No |
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|
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N D. |
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● |
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N.D.= Not Determined; F = Frozen sections; FC = Flow Cytometry; FS = Functional Studies; IA = Immuno Assays; IF = Immuno Fluorescence; IP = Immuno Precipitation; P = Paraffin sections; W = Western blot
Application F has been tested by Hycult Biotech.
Application notes
F: Cryostat sections (7µm) of mouse tissue were acetone fixed and stained o/n at 4°C in TBS/2% goat serum. (Ref.4)
IA: Biotinylated 14D12 was used as detector in ELISA at 1µg/ml TBS/Tween-20/Ca (Ref.1)
IF: Hyphae of C. albicans were fixed on poly-l-lysin coated slides with ice-cold aceton. Slides were incubated for 1h at RT with 14D12. (Ref.3)
W: On a 12% non-reducing SDS-PAGE a prominent band of ca. 50Kda is detected. Under reducing conditions a 26 KDa band is detected. (Ref.2)
MBL-C (clone 14D12) deposition in developing murine atherosclerotic lesions following 10 weeks of high fat feeding. MBL-C was detected in and around invading macrophages invading the intima (insert). MBL-C bound, similar to MBL-A, at sites of necrosis (upper right corner). No MBL-C binding was shown in the media or on fibrous caps covering the thickened intima.
IA: Biotinylated 14D12 was used as detector in ELISA at 1µg/ml TBS/Tween-20/Ca (Ref.1)
IF: Hyphae of C. albicans were fixed on poly-l-lysin coated slides with ice-cold aceton. Slides were incubated for 1h at RT with 14D12. (Ref.3)
W: On a 12% non-reducing SDS-PAGE a prominent band of ca. 50Kda is detected. Under reducing conditions a 26 KDa band is detected. (Ref.2)
MBL-C (clone 14D12) deposition in developing murine atherosclerotic lesions following 10 weeks of high fat feeding. MBL-C was detected in and around invading macrophages invading the intima (insert). MBL-C bound, similar to MBL-A, at sites of necrosis (upper right corner). No MBL-C binding was shown in the media or on fibrous caps covering the thickened intima.
Use
For immuno histology and Western blotting dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:10. It is recommended that solutions with a calcium concentration of 1 mM are used (14D12 is a calcium-dependent antibody).
Aliases
MBL, L-MB, MBL-C, MBP-C, Mbl2
Positive control
Mouse Serum and kidney tissue
Storage and stability
Product should be stored at 4°C. Under recommended storage conditions, product is stable for one year.
References
1. Liu, H et al; Characterization and quantification of mouse mannan-binding lectins (MBL-A and MBL-C) and study of acute phase responses. Scand J Immunol 2001, 53: 489
2. Phaneuf, L et al; Binding of mouse mannan-binding lectin to different bacterial pathogens of mice. Vet Immunol Immunopathol 2007, 118: 129
3. Held, K et al; Increased susceptibility of complement factor B/C2 double knockout mice and mannan binding lectin knockout mice to systemic infection with Candida albicans. Mol Immunol 2008, 45: 3934
4. Matthijsen, R et al; Macrophage-specific expression of mannose-binding lectin controls atherosclerosis in low-density lipoprotein receptor deficient mice. Circulation 2009, 119: 2188
5. Pumidonming, W et al, Binding to complement factors and activation of the alternative pathway by Acanthamoeba. Immunobiol. 2010, 216: 225
2. Phaneuf, L et al; Binding of mouse mannan-binding lectin to different bacterial pathogens of mice. Vet Immunol Immunopathol 2007, 118: 129
3. Held, K et al; Increased susceptibility of complement factor B/C2 double knockout mice and mannan binding lectin knockout mice to systemic infection with Candida albicans. Mol Immunol 2008, 45: 3934
4. Matthijsen, R et al; Macrophage-specific expression of mannose-binding lectin controls atherosclerosis in low-density lipoprotein receptor deficient mice. Circulation 2009, 119: 2188
5. Pumidonming, W et al, Binding to complement factors and activation of the alternative pathway by Acanthamoeba. Immunobiol. 2010, 216: 225
Precautions
For research use only. Not for use in or on humans or animals or for diagnostics. It is the responsibility of the user to comply with all local/state and Federal rules in the use of this product. Hycult Biotech is not responsible for any patent infringements that might result with the use of or derivation of this product.
Also available
| HM1035 | MBL-A, Mouse, mAb 8G6 |
| HM1036 | MBL-A, Mouse, mAb 2B4 |
| HM1037 | MBL-C, Mouse, mAb 16A8 |
References
1. Liu, H et al; Characterization and quantification of mouse mannan-binding lectins (MBL-A and MBL-C) and study of acute phase responses. Scand J Immunol 2001, 53: 489
2. Phaneuf, L et al; Binding of mouse mannan-binding lectin to different bacterial pathogens of mice. Vet Immunol Immunopathol 2007, 118: 129
3. Held, K et al; Increased susceptibility of complement factor B/C2 double knockout mice and mannan binding lectin knockout mice to systemic infection with Candida albicans. Mol Immunol 2008, 45: 3934
4. Matthijsen, R et al; Macrophage-specific expression of mannose-binding lectin controls atherosclerosis in low-density lipoprotein receptor deficient mice. Circulation 2009, 119: 2188
5. Pumidonming, W et al, Binding to complement factors and activation of the alternative pathway by Acanthamoeba. Immunobiol. 2010, 216: 225
2. Phaneuf, L et al; Binding of mouse mannan-binding lectin to different bacterial pathogens of mice. Vet Immunol Immunopathol 2007, 118: 129
3. Held, K et al; Increased susceptibility of complement factor B/C2 double knockout mice and mannan binding lectin knockout mice to systemic infection with Candida albicans. Mol Immunol 2008, 45: 3934
4. Matthijsen, R et al; Macrophage-specific expression of mannose-binding lectin controls atherosclerosis in low-density lipoprotein receptor deficient mice. Circulation 2009, 119: 2188
5. Pumidonming, W et al, Binding to complement factors and activation of the alternative pathway by Acanthamoeba. Immunobiol. 2010, 216: 225
Protocols
Protocols
Protocols
| Related products | Cat # | |
|---|---|---|
| MBL-A, Mouse, mAb 2B4 | HM1036 | |
| MBL-C, Mouse, mAb 16A8 | HM1037 | |
| MBL-A, Mouse, mAb 8G6 | HM1035 | |